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Biochemistry|August 27, 2014
Yeast alcohol dehydrogenase structure and catalysisSavarimuthu Baskar Raj, S Ramaswamy, Bryce V PlappBiochemistry|April 26, 2012
Atomic-resolution structures of horse liver alcohol dehydrogenase with NAD(+) and fluoroalcohols define strained Michaelis complexesBryce V Plapp, S RamaswamyArchives of Biochemistry and Biophysics|January 9, 2016
Mechanistic implications from structures of yeast alcohol dehydrogenase complexed with coenzyme and an alcoholBryce V Plapp, Henry A Charlier, S RamaswamyBiochemistry|March 17, 2004
Participation of histidine-51 in catalysis by horse liver alcohol dehydrogenaseLaurie A LeBrun, Doo-Hong Park, S Ramaswamy, et al.Archives of Biochemistry and Biophysics|July 9, 2009
Conformational changes and catalysis by alcohol dehydrogenaseBryce V PlappChemico-Biological Interactions|December 27, 2023
Solvent isotope and mutagenesis studies on the proton relay system in yeast alcohol dehydrogenase 1Bryce V PlappChemico-Biological Interactions|September 16, 2021
The Thr45Gly substitution in yeast alcohol dehydrogenase substantially decreases catalysis, alters pH dependencies, and disrupts the proton relay systemSuresh Pal, Bryce V PlappChemico-Biological Interactions|December 28, 2016
Inversion of substrate stereoselectivity of horse liver alcohol dehydrogenase by substitutions of Ser-48 and Phe-93Keehyuk Kim, Bryce V PlappBiochemistry|January 30, 2020
Substitutions of Amino Acid Residues in the Substrate Binding Site of Horse Liver Alcohol Dehydrogenase Have Small Effects on the Structures but Significantly Affect Catalysis of Hydrogen TransferKeehyuk Kim, Bryce V PlappChemico-Biological Interactions|February 6, 2019
Substitution of cysteine-153 ligated to the catalytic zinc in yeast alcohol dehydrogenase with aspartic acid and analysis of mechanisms of related medium chain dehydrogenasesKeehyuk Kim, Bryce V PlappPageof 36